Effect of Alkylating Agents on the Expression of Inducible Genes of Escherichia coli

References

1. Anderson W. F., Takeda Y., Ohlendorf D. H., Matthews B. W. 1982; Proposed α-helical super-secondary structure associated with protein–DNA recognition. Journal of Molecular Biology 159:745–751
   [Google Scholar]
2. Auerbach C. 1976; In Mutation Research: Problems, Results, and Perspectives. pp 504–553 London: Chapman & Hall;
   [Google Scholar]
3. Barbé J., Vericat J. A., Guerrero R. 1983; Discriminated induction of SOS functions in Escherichia coli by alkylating agents. Journal of General Microbiology 129:2079–2089
   [Google Scholar]
4. Barbé, J., Cairó J., Vericat J. A., Guerrero R. 1985; Further characterization of SOS system in recBC mutants of Escherichia coli. Mutation Research 146:23–32
   [Google Scholar]
5. Clark D. J., Maaløe O. 1967; DNA replication and the division cycle of Escherichia coli. Journal of Molecular Biology 23:99–112
   [Google Scholar]
6. Crooke S. T. 1981; Mitomycin C; an overview. In Cancer and Chemotherapy vol. 3 pp. 49–60 Edited by Crooke S. T., Prestayco A. W. New York: Academic Press;
   [Google Scholar]
7. D’Andrea A. D., Haseltine W. A. 1978; Sequence specific cleavage of DNA by the antitumor antibiotics neocarzinostatin and bleomycin. Proceedings of the National Academy of Sciences of the United States of America 75:3608–3612
   [Google Scholar]
8. Guerrero R., Barbé J. 1982; Expression of recA-gene dependent SOS functions in Salmonella typhimurium. Antonie van Leeuwenhoek 48:159–167
   [Google Scholar]
9. Helène C. 1977; Specific recognition of guanine bases in protein–nucleic acid complexes. FEBS Letters 74:10–13
   [Google Scholar]
10. Hoffmann G. R. 1980; Genetic effects of dimethyl sulfate, diethyl sulfate and related compounds. Mutation Research 75:63–129
    [Google Scholar]
11. Jeggo P., Defais M., Samson L., Schendel P. 1977; An adaptive response of E. coli to low levels of alkylating agents: comparison with previously characterized DNA repair pathways. Molecular and General Genetics 157:1–9
    [Google Scholar]
12. Kenyon C. J., Walker G. C. 1981; Expression of the E. coli uvrA gene is inducible. Nature, London 289:808–810
    [Google Scholar]
13. Kunkel G. R., Martinson H. G. 1978; Histone–DNA interactions within chromatin. Isolation of histones from DNA–histone adducts induced in nuclei by UV light. Nucleic Acids Research 5:4263–4272
    [Google Scholar]
14. Lawley P. D. 1974; Some chemical aspects of dose-response relationships in alkylating mutagenesis. Mutation Research 23:283–295
    [Google Scholar]
15. Lawley P. D., Orr D. J. 1970; Specific excision of methylation products from DNA of Escherichia coli treated with N-methyl-N′-nitro-N-nitrosoguanidine. Chemico-Biological Interactions 2:154–157
    [Google Scholar]
16. Lin S.-Y., Riggs A. D. 1972; Lac operator analogues: bromodeoxyuridine substitution in the lac operator affects the rate of dissociation of the lac repressor. Proceedings of the National Academy of Sciences of the United States of America 69:2574–2576
    [Google Scholar]
17. Lin S.-Y., Riggs A. D. 1976; The binding of lac repressor and the catabolite gene activator protein to halogen-substituted analogues of poly [d(A-T)]. Biochimica et biophysica acta 432:185–191
    [Google Scholar]
18. Little J. W., Mount D. W. 1982; The SOS regulatory system of Escherichia coli. Cell 29:11–22
    [Google Scholar]
19. Little J. W., Edmiston S. M., Pacelli L. Z., Mount D. W. 1980; Cleavage of the Escherichia coli LexA protein by the RecA protease. Proceedings of the National Academy of Sciences of the United States of America 77:3225–3229
    [Google Scholar]
20. Markovitz A. 1972; Ultraviolet light-induced stable complexes on DNA and DNA polymerase. Biochimica et biophysica acta 281:522–534
    [Google Scholar]
21. Matthews B. W., Ohlendorf D. H., Anderson W. F., Fisher R. G., Takeda Y. 1983; Cro repressor protein and its interaction with DNA. Cold Spring Harbor Symposia on Quantitative Biology 47:427–433
    [Google Scholar]
22. Miller J. M. 1972; Experiments in Molecular Genetics. Cold Spring Harbor New York: Cold Spring Harbor Laboratories;
    [Google Scholar]
23. Moreau P. L., Fanica M., Devoret R. 1980; Induction of prophage lambda does not require full induction of recA protein synthesis. Biochimie 62:687–694
    [Google Scholar]
24. Ohta T., Nakamura N., Moriya M., Shirasu Y., Kada T. 1984; The SOS-function-inducing activity of chemical mutagens in Escherichia coli. Mutation Research 131:101–109
    [Google Scholar]
25. Oishi M., Smith C. L., Friefeld B. 1979; Molecular events and molecules that lead to induction of prophage and SOS functions. Cold Spring Harbor Symposia on Quantitative Biology 43:897–907
    [Google Scholar]
26. Pabo C. O., Lewis M. 1982; The operator-binding domain of λ repressor: structure and DNA recognition. Nature, London 298:441–443
    [Google Scholar]
27. Pabo C. O., Krovatin W., Jeffrey A., Sauer R. T. 1982; The N-terminal arms of λ repressor wrap around the operator DNA. Nature, London 298:444–446
    [Google Scholar]
28. Roberts J. W., Roberts C. W., Craig N. L. 1978; Escherichia coli recA gene product inactivates phage λ repressor. Proceedings of the National Academy of Sciences of the United States of America 75:4714–4718
    [Google Scholar]
29. Sauer R. T., Pabo C. O., Meyer B. J., Ptashne M., Backman K. C. 1979; Regulatory functions of the λ repressor reside in the amino-terminal domain. Nature, London 279:396–400
    [Google Scholar]
30. Sauer R. T., Yocum R. R., Doolittle R. F., Lewis M., Pabo C. O. 1982a; Homology among DNA-binding proteins suggest use of a conserved super-secondary structure. Nature, London 298:447–451
    [Google Scholar]
31. Sauer R. T., Ross M. J., Ptashne M. 1982b; Cleavage of the λ and P22 repressors by recA protein. Journal of Biological Chemistry 257:4458–4462
    [Google Scholar]
32. Schendel P. F., Fogliano M., Strausbaugh L. D. 1982; Regulation of the Escherichia coli K12 uvrB operon. Journal of Bacteriology 150:676–685
    [Google Scholar]
33. Simic M. G., Dizdaroglu M. 1985; Formation of radiation-induced cross-links between thymine and tyrosine: possible model for cross-linking of DNA and proteins by ionizing radiation. Biochemistry 24:233–236
    [Google Scholar]
34. Smith T. F., Sadler J. R. 1971; The nature of lactose operator constitutive mutants. Journal of Molecular Biology 59:273–305
    [Google Scholar]
35. Smith C. L., Siegfried E., Ruvolo P. P. 1983; Adaptive doses of MNNG induce a recA-trp gene fusion. DNA 2:291–299
    [Google Scholar]
36. Steitz T. A., Weber I. T., Mathew J. B. 1983; Catabolite gene activator protein: structure, homology with other proteins, and cyclic AMP and DNA binding. Cold Spring Harbor Symposia on Quantitative Biology 47:419–426
    [Google Scholar]
37. Vericat J. A., Barbé J., Guerrero R. 1984; Expression of the SOS response following simultaneous treatment with methyl-nitrosoguanidine and mitomycin C in Escherichia coli. Mutation Research 132:15–20
    [Google Scholar]
38. Walker G. C. 1984; Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli. Microbiological Reviews 48:60–93
    [Google Scholar]
39. Witkin E. M. 1974; Thermal enhancement of ultraviolet mutability in a tif uvrA derivative of Escherichia coli B/r: evidence that ultraviolet mutagenesis depends on an inducible function. Proceedings of the National Academy of Sciences of the United States of America 71:1930–1934
    [Google Scholar]
40. Yoda K., Sakiyama S., Fujimura S. 1982; Interaction of N-ethyl-N′-nitro-N-nitrosoguanidine with nucleic acids and proteins in comparison with N-methyl-N′-nitro-N-nitrosoguanidine. Chemico-Biological Interactions 41:49–59
    [Google Scholar]